ID   A0A0X3YAG3_9GAMM        Unreviewed;       549 AA.
AC   A0A0X3YAG3;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:KUM53835.1};
DE            EC=5.4.2.2 {ECO:0000313|EMBL:KUM53835.1};
GN   ORFNames=AR688_19475 {ECO:0000313|EMBL:KUM53835.1};
OS   Rheinheimera sp. EpRS3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Rheinheimera.
OX   NCBI_TaxID=1712383 {ECO:0000313|EMBL:KUM53835.1, ECO:0000313|Proteomes:UP000054239};
RN   [1] {ECO:0000313|Proteomes:UP000054239}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS3 {ECO:0000313|Proteomes:UP000054239};
RA   Presta L., Bosi E., Fondi M., Maida I., Maggini V., Bogani P.,
RA   Firenzuoli F., Chiellini C., De Pascale D., Palma F., Di Pilato V.,
RA   Rossolini G., Mengoni A., Fani R.;
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|RuleBase:RU004326}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUM53835.1}.
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DR   EMBL; LNQS01000007; KUM53835.1; -; Genomic_DNA.
DR   RefSeq; WP_068231884.1; NZ_LNQS01000007.1.
DR   AlphaFoldDB; A0A0X3YAG3; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000054239; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd05801; PGM_like3; 1.
DR   Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
DR   Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 1.
DR   InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR   InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR   InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR   InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR   InterPro; IPR005843; A-D-PHexomutase_C.
DR   InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR   InterPro; IPR016066; A-D-PHexomutase_CS.
DR   InterPro; IPR005852; PGM_a-D-Glc-sp.
DR   NCBIfam; TIGR01132; pgm; 1.
DR   PANTHER; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2A-RELATED; 1.
DR   PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 1.
DR   Pfam; PF02878; PGM_PMM_I; 1.
DR   Pfam; PF02879; PGM_PMM_II; 1.
DR   Pfam; PF02880; PGM_PMM_III; 1.
DR   Pfam; PF00408; PGM_PMM_IV; 1.
DR   SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:KUM53835.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004326};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004326};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          41..181
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          212..319
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          323..440
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          481..539
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   549 AA;  59375 MW;  7921AE1DB5B55C93 CRC64;
     MSLHPLAGQQ VPTSLVPNIS RLMTAYYVLE PDVHTQPEHK VSFGTSGHRG SALNCSFNEP
     HVLAICQAVA DYRKKNAITG PLFLGKDTHA LSEAAFATAL EVLIANKIQV CIQKDLGYTP
     TPVISHAILT QNKGATSQLA DGIVITPSHN PPQDGGIKYN PPHGGPADTD VTNWIEQRAN
     ELLAKDLEGV KMMPYALALQ SGYCQHIDYI QHYVDDLANV IDMAAIAKAG IKIGVDPLGG
     SGIAYWPRIA ERYGLNITVV NEKVDPAFAF MPLDKDGQIR MDCSSAYAMA NLIQLKDQFD
     IAIGNDPDFD RHGIVTRSGG LMNPNHYLAV AINYLLANRP DWAAELAIGK TLVSSALIDR
     VVAARGRNLL EVPVGFKWFV EGLHNGSVAF GGEESAGASF LRFDGSAWST DKDGIILGLL
     AAEMLAKTGV DPYQQYQALT RELGSPLYRR LDAPASSEQK AALKKLDVKS VKQTTLAGDD
     ILAVLTKAPG NNADIGGVKV VTRNGWFAAR PSGTENSYKI YLESFVDQGH LLQLEHDAKA
     FVEYVFSQI
//